EMDB EMD-9045

Single particle reconstruction
4.17Å resolution

Yeast 26S proteasome bound to ubiquitinated substrate (4D motor state)

Map released:
Last modified:
Overview of EMD-9045
Source organisms:
Fitted atomic model: 6ef3
Related EM entries by publication: EMD-9042, EMD-9043, EMD-9044
Primary publication:
Substrate-engaged 26Sproteasome structures reveal mechanisms for ATP-hydrolysis-driven translocation.
de la Pena AH, Goodall EA, Gates SN, Lander GC, Martin A
Science 362 - (2018)
PMID: 30309908

Function and Biology Details

Sample name: Substrate-engaged 26S proteasome in the 4D state
Ligands: ADENOSINE-5'-TRIPHOSPHATE, ADENOSINE-5'-DIPHOSPHATE
Proteins: Substrate-engaged 26S proteasome in the 4D state, Proteasome, substrate, Proteasome subunit beta type-1, Proteasome subunit beta type-2, Proteasome subunit beta type-3, Proteasome subunit beta type-4, Proteasome subunit beta type-5, Proteasome subunit beta type-6, Proteasome subunit beta type-7, Proteasome subunit alpha type-1, Proteasome subunit alpha type-2, Proteasome subunit alpha type-3, Proteasome subunit alpha type-4, Proteasome subunit alpha type-5, Proteasome subunit alpha type-6, Probable proteasome subunit alpha type-7, 26S proteasome regulatory subunit 7 homolog, 26S proteasome regulatory subunit 4 homolog, 26S proteasome regulatory subunit 8 homolog, 26S proteasome regulatory subunit 6B homolog, 26S proteasome subunit RPT4, 26S proteasome regulatory subunit 6A, Proteasome subunit beta type-7, Ubiquitin carboxyl-terminal hydrolase RPN11, Model substrate polypeptide, Ubiquitin-60S ribosomal protein L40

Experimental Information Details

Resolution: 4.17Å
Resolution method: FSC 0.143 CUT-OFF
Applied symmetry: C1
Reconstruction software: RELION
Microscope: FEI TITAN KRIOS
Detector: GATAN K2 SUMMIT (4k x 4k)